Toward an understanding of autophagosomelysosome fusion: The unsuspected role of ATG14

Autophagy

Volumn 11, Issue 4, 2015, Pages 583-584

  Bernard, Amélie ^a   Klionsky, Daniel J ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

Autophagy; Fusion; Lysosome; SNARE; Stress

Indexed keywords

ATG14 PROTEIN; PEPTIDES AND PROTEINS; SYNTAXIN; SYNTAXIN 17; UNCLASSIFIED DRUG; SNARE PROTEIN;

AUTOPHAGOSOME; AUTOPHAGY; LYSOSOME; MEMBRANE FUSION; MEMBRANE VESICLE; NOTE; PROTEIN PROTEIN INTERACTION; ANIMAL; HUMAN; METABOLISM; PHAGOSOME; PHYSIOLOGY;

ANIMALS; AUTOPHAGY; HUMANS; LYSOSOMES; MEMBRANE FUSION; PHAGOSOMES; SNARE PROTEINS;

EID: 84953880644     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2015.1029220     Document Type: Note

References (3)

1. Diao J, Liu R, Rong Y, Zhao M, Zhang J, Lai Y, Zhou Q, Wilz LM, Li J, Vivona S, et al. ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes. Nature 2015; in press; PMID:25686604; http://dx.doi.org/10.1038/nature14147.
2. Hamasaki M, Furuta N, Matsuda A, Nezu A, Yamamoto A, Fujita N, Oomori H, Noda T, Haraguchi T, Hiraoka Y, et al. Autophagosomes form at ER-mitochondria contact sites. Nature 2013; 495:389-393; PMID:23455425; http://dx.doi.org/10.1038/nature11910.
3. Itakura E, Itakura CK, Mizushima N. The hairpin-type tail-anchored SNARE Syntaxin17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 2012; 151:1256-1269; PMID:23217709; http://dx.doi.org/10.1016/j.cell.2012.11.001.